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1VR7

Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from THERMOTOGA MARITIMA at 1.2 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004014molecular_functionadenosylmethionine decarboxylase activity
A0005829cellular_componentcytosol
A0008295biological_processspermidine biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
B0004014molecular_functionadenosylmethionine decarboxylase activity
B0005829cellular_componentcytosol
B0008295biological_processspermidine biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 131
ChainResidue
AVAL9
AGLU11
AHIS106
BHIS110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000250
ChainResidueDetails
ASER63
BSER63

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor; for processing activity => ECO:0000305|PubMed:15150268
ChainResidueDetails
AHIS68
BHIS68

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor; for catalytic activity => ECO:0000305|PubMed:15150268
ChainResidueDetails
ACYS83
BCYS83

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Cleavage (non-hydrolytic); by autolysis => ECO:0000305
ChainResidueDetails
AGLU62
BGLU62

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Pyruvic acid (Ser); by autocatalysis => ECO:0000305
ChainResidueDetails
ASER63
BSER63

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 225
ChainResidueDetails
ASER55electrostatic stabiliser
AGLU62covalently attached, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
ASER63covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleophile, polar interaction, proton donor
AHIS68hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS83hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 225
ChainResidueDetails
BSER55electrostatic stabiliser
BGLU62covalently attached, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
BSER63covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleophile, polar interaction, proton donor
BHIS68hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS83hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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